Atomistry » Magnesium » PDB 7cu9-7d8g » 7cvm
Atomistry »
  Magnesium »
    PDB 7cu9-7d8g »
      7cvm »

Magnesium in PDB 7cvm: Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms)

Enzymatic activity of Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms)

All present enzymatic activity of Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms):
5.3.1.5;

Protein crystallography data

The structure of Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms), PDB code: 7cvm was solved by K.H.Nam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.05 / 2.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.550, 100.260, 103.610, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 24.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms) (pdb code 7cvm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms), PDB code: 7cvm:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7cvm

Go back to Magnesium Binding Sites List in 7cvm
Magnesium binding site 1 out of 2 in the Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:9.3
occ:1.00
O A:HOH659 2.0 17.0 1.0
OE1 A:GLU217 2.1 16.6 1.0
OD2 A:ASP255 2.1 22.8 1.0
OD1 A:ASP257 2.4 16.4 1.0
OD1 A:ASP255 2.6 18.8 1.0
NE2 A:HIS220 2.7 13.1 1.0
CG A:ASP255 2.7 16.8 1.0
CD A:GLU217 3.1 12.6 1.0
CD2 A:HIS220 3.2 11.4 1.0
CG A:ASP257 3.3 14.0 1.0
OD2 A:ASP257 3.4 25.0 1.0
OE2 A:GLU217 3.6 15.6 1.0
O A:HOH747 3.7 19.7 1.0
CE1 A:HIS220 3.8 13.0 1.0
ND2 A:ASN247 4.0 16.8 1.0
CB A:ASP255 4.2 15.6 1.0
O A:HOH566 4.2 18.0 1.0
CG A:HIS220 4.4 11.4 1.0
CG A:GLU217 4.4 10.8 1.0
ND1 A:HIS220 4.7 9.9 1.0
CB A:ASP257 4.7 15.0 1.0
NZ A:LYS183 4.7 20.2 1.0
OD2 A:ASP287 4.7 17.8 1.0
CE A:LYS183 4.8 14.1 1.0
O A:HOH554 4.8 32.8 1.0
MG A:MG402 4.9 16.5 1.0
O A:HOH508 5.0 31.6 1.0

Magnesium binding site 2 out of 2 in 7cvm

Go back to Magnesium Binding Sites List in 7cvm
Magnesium binding site 2 out of 2 in the Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Glucose Isomerase By Fixed-Target Serial Synchrotron Crystallography (500 Ms) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:16.5
occ:1.00
OE2 A:GLU217 1.9 15.6 1.0
OD2 A:ASP287 2.2 17.8 1.0
OD2 A:ASP245 2.5 18.4 1.0
OE1 A:GLU181 2.6 28.6 1.0
O A:HOH508 2.8 31.6 1.0
CD A:GLU217 3.1 12.6 1.0
CD A:GLU181 3.2 22.5 1.0
CG A:ASP287 3.3 18.3 1.0
O A:HOH589 3.5 31.6 1.0
OE2 A:GLU181 3.5 21.5 1.0
CG A:ASP245 3.5 19.1 1.0
CB A:ASP287 3.7 13.3 1.0
O A:HOH545 3.8 30.7 1.0
CB A:ASP245 3.9 12.6 1.0
CG A:GLU217 4.0 10.8 1.0
OE1 A:GLU217 4.0 16.6 1.0
CB A:GLU217 4.1 12.3 1.0
O A:HOH659 4.1 17.0 1.0
CE1 A:HIS220 4.2 13.0 1.0
CG A:GLU181 4.4 16.3 1.0
OD1 A:ASP287 4.4 17.5 1.0
NE2 A:HIS220 4.6 13.1 1.0
OD1 A:ASP245 4.6 21.6 1.0
MG A:MG401 4.9 9.3 1.0
ND1 A:HIS220 4.9 9.9 1.0

Reference:

K.H.Nam, K.H.Nam. N/A N/A.
Page generated: Wed Oct 2 14:39:57 2024

Last articles

Mg in 1VQ9
Mg in 1VQ7
Mg in 1VQ5
Mg in 1VQ6
Mg in 1VQ8
Mg in 1VQ4
Mg in 1VPA
Mg in 1VPE
Mg in 1VOM
Mg in 1VMA
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy